VAMP-1/2 Antibody (SP11): sc-56609

VAMP-1/2 Antibody (SP11) is a mouse monoclonal IgG1 antibody that detects VAMP-1/2 in human and porcine samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and immunohistochemistry. VAMP-1/2, also known as synaptobrevins, are integral components of the vesicle trafficking machinery, playing a crucial role in the process of exocytosis, which is essential for neurotransmitter release and various cellular signaling pathways. These proteins are primarily located on the membranes of synaptic vesicles and are vital for the fusion of these vesicles with the presynaptic membrane, facilitating the release of neurotransmitters into the synaptic cleft. The interaction of VAMP-1/2 with syntaxins and SNAPs is critical for the formation of the SNARE complex, which drives membrane fusion. Disruption of this process can lead to significant neurological disorders, highlighting the importance of VAMP-1/2 in maintaining synaptic function and communication. Anti-VAMP-1/2 antibody (SP11) is an invaluable tool for researchers studying synaptic transmission and related cellular processes, providing insights into the molecular mechanisms underlying neurotransmitter release and potential therapeutic targets for neurological diseases.

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VAMP-1/2 Antibody (SP11) References:

1. The cytoplasmic domain of Vamp4 and Vamp5 is responsible for their correct subcellular targeting: the N-terminal extenSion of VAMP4 contains a dominant autonomous targeting signal for the trans-Golgi network.  |  Zeng, Q., et al. 2003. J Biol Chem. 278: 23046-54. PMID: 12682051
2. Heterogeneity of glutamatergic and GABAergic release machinery in cerebral cortex: analysis of synaptogyrin, vesicle-associated membrane protein, and syntaxin.  |  Bragina, L., et al. 2010. Neuroscience. 165: 934-43. PMID: 19909789
3. Striatal synaptosomes from Hdh140Q/140Q knock-in mice have altered protein levels, novel sites of methionine oxidation, and excess glutamate release after stimulation.  |  Valencia, A., et al. 2013. J Huntingtons Dis. 2: 459-75. PMID: 24696705
4. APP is cleaved by Bace1 in pre-synaptic vesicles and establishes a pre-synaptic interactome, via its intracellular domain, with molecular complexes that regulate pre-synaptic vesicles functions.  |  Del Prete, D., et al. 2014. PLoS One. 9: e108576. PMID: 25247712
5. Differences in human cortical gene expression match the temporal properties of large-scale functional networks.  |  Cioli, C., et al. 2014. PLoS One. 9: e115913. PMID: 25546015
6. Soluble N-ethylmaleimide-sensitive Factor Attachment Receptor (SNARE) Protein Involved in the Remission of Depression by Acupuncture in Rats.  |  Fan, L., et al. 2016. J Acupunct Meridian Stud. 9: 242-249. PMID: 27776762
7. Involvement of SNARE complex in the hippocampus and prefrontal cortex of offspring with depression induced by prenatal stress.  |  Cao, YJ., et al. 2018. J Affect Disord. 235: 374-383. PMID: 29674253
8. The glucose transporter (GLUT-4) and vesicle-associated membrane protein-2 (VAMP-2) are segregated from recycling endosomes in insulin-sensitive cells.  |  Martin, S., et al. 1996. J Cell Biol. 134: 625-35. PMID: 8707843
9. Vesicle-associated membrane protein 2 plays a specific role in the insulin-dependent trafficking of the facilitative glucose transporter GLUT4 in 3T3-L1 adipocytes.  |  Martin, LB., et al. 1998. J Biol Chem. 273: 1444-52. PMID: 9430681
10. VAMP-1 and VAMP-2 gene expression in rat spinal motoneurones: differential regulation after neuronal injury.  |  Jacobsson, G., et al. 1998. Eur J Neurosci. 10: 301-16. PMID: 9753139

The preferred VAMP-2 antibody is VAMP-2 Antibody (3E5): sc-69706.